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First published online 20 March 2007
doi: 10.1242/jcs.004291
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Research Article |
1 Department of Cell Biology, Albert Einstein College of Medicine, New York, NY 10461, USA
2 Cardiovascular Biology Research Program, Oklahoma Medical Research Foundation, Oklahoma City, OK 73104, USA
3 Department of Biochemistry and Molecular Biology, Oklahoma Center for Medical Glycobiology, University of Oklahoma Health Sciences Center, Oklahoma City, OK 73104, USA
Author for correspondence (e-mail: stanley{at}aecom.yu.edu)
Accepted 13 February 2007
Fertilization in mammals requires sperm to bind to the zona pellucida (ZP) that surrounds the egg. Galactose (Gal) or N-acetylglucosamine (GlcNAc) residues on the glycans of ZP protein 3 (ZP3) have been implicated as mouse sperm receptors. However, Mgat1–/– eggs with modified N-glycans lacking terminal Gal and GlcNAc residues are fertilized. To determine if Gal and GlcNAc on O-glycans of the ZP are required for fertilization, a conditional allele of the T-synthase gene (T-synF) was generated. T-syn encodes core 1 
1,3-galactosyltransferase 1 (T-synthase), which initiates the synthesis of core-1-derived O-glycans, the only O-glycans on mouse ZP3. T-synF/F:ZP3Cre females in which T-synF was deleted at the beginning of oogenesis generated eggs lacking core-1-derived O-glycans. Nevertheless, T-synF/F:ZP3Cre females were fertile and their eggs bound sperm similarly to controls. In addition, T-syn–/– embryos generated from T-syn null eggs developed until 
E12.5. Thus, core-1-derived O-glycans are not required for blastogenesis, implantation, or development prior to midgestation. Moreover, T-syn–/–Mgat1–/– eggs lacking complex and hybrid N-glycans as well as core-1-derived O-glycans were fertilized. The combined data show that mouse ZP3 does not require terminal Gal or GlcNAc on either N- or O-glycans for fertilization.
Key words: Fertilization, Zona pelucida, O-glycans, N-glycans, T-synthase
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